PMC:4502370 / 42172-42995 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/4502370","sourcedb":"PMC","sourceid":"4502370","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4502370","text":"The C-terminal 77-aa segment of yeast Snp1 is rich in arginine (n = 11), serine (n = 12), and alanine (n = 11) and is predicted to be strongly hydrophilic, with the exception of one hydrophobic tract (265PLLSAATPTAAVTSVY280). The amino acid sequence and composition are suggestive of structural disorder or a structure that is templated by the association of this polypeptide with other proteins. Because this segment is not conserved in human U1-70K and the C-terminus of U1-70K is not seen in U1 snRNP crystal structures, we cannot intuit what contacts might be made by the Snp1 C-terminus. This will be an interesting topic for future studies given the broad impact, both positive and negative, of Snp1 C-terminal deletion on yeast physiology when other components of the splicing apparatus are simultaneously perturbed.","tracks":[]}